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The mongoose acetylcholine receptor α‐subunit: analysis of glycosylation and α‐bungarotoxin binding
Author(s) -
Asher Orna,
Jensen Bo S,
Lupu-Meiri Monica,
Oron Yoram,
Fuchs Sara
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00341-x
Subject(s) - mongoose , glycosylation , protein subunit , interleukin 10 receptor, alpha subunit , g alpha subunit , acetylcholine receptor , biochemistry , alpha (finance) , biology , interleukin 5 receptor alpha subunit , binding site , receptor , chemistry , microbiology and biotechnology , medicine , ecology , construct validity , nursing , patient satisfaction , gene
The mongoose AChR α‐subunit has been cloned and shown to be highly homologous to other AChR α‐subunits, with only six differences in amino acid residues at positions that are conserved in animal species that bind α‐bungarotoxin (α‐BTX). Four of these six substitutions cluster in the ligand binding site, and one of them, Asn‐187, forms a consensus N‐glycosylation site. The mongoose glycosylated α‐subunit has a higher apparent molecular mass than that of the rat glycosylated α‐subunit, probably resulting from the additional glycosylation at Asn‐187 of the mongoose subunit. The in vitro translated mongoose α‐subunit, in a glycosylated or non‐glycosylated form, does not bind α‐BTX, indicating that lack of α‐BTX binding can be achieved also in the absence of glycosylation.